ID B8N4G8_ASPFN Unreviewed; 572 AA.
AC B8N4G8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Calpain-like protein {ECO:0000313|EMBL:EED56399.1};
GN ORFNames=AFLA_036710 {ECO:0000313|EMBL:EED56399.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED56399.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED56399.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; EQ963473; EED56399.1; -; Genomic_DNA.
DR RefSeq; XP_002375181.1; XM_002375140.1.
DR AlphaFoldDB; B8N4G8; -.
DR STRING; 332952.B8N4G8; -.
DR EnsemblFungi; EED56399; EED56399; AFLA_036710.
DR VEuPathDB; FungiDB:AFLA_001559; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_006072_3_3_1; -.
DR OMA; ENDASRC; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF00648; Peptidase_C2; 2.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 141..439
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 363
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 572 AA; 66051 MW; 8F3AEBA03A625136 CRC64;
MDHDDDLTDM VFTPPLSTRS GGRKRRASQT PQETLRQFWN QFNSKFPGRV YTVLPDNPYA
RTKAERAPKG VIQGQDAGKS YEEARKECRR AVDRIVKECE RLNQKYTDPH FDIEVDLKSG
KRNCLDTLEE ENMEMRPRGV KRVTEIFEKP RFFVNGPTAS DVRQGRDGDC WFMAALCTMG
NKQGLIEQIC VARDEKIGVY GFVFYRDGEW QQCIVDDKLY LRAADYDESV DERPIWDDIN
RADTEEEYRK VWQTGSRALY FARCVDENET WLPLLEKAYA KAHGDFSAIE GGFVGEAIED
LTGGVTSEIL SSSILDKDRF WKEELMKVNK EFLFGCGTGL YSNWLDPKYR GPPRDRKGIS
ENHSYSIMDA KEIDGERLLR LRNPWGKKEW TGAWSDGSEQ WTPEWMEKLG HKFGNDGFFW
ISYDDLLKKY QHFDRTRLFG PEWSIAQQWT TVNVPWSADY HSTKFMVNVT KAGPVVLVLS
QFRVQKEGED DYMVRSQSSH LICRSVNAEV DLEPGRYHVL MKVTAYRNGE MESTEEALSL
EVVRSVSKRD TGAALDMDDP LKSASFSRLE AN
//
